RUVBL1/2 in complex with ATP. Determined by electron microscopy at 3.26 Å resolution. Released 15 May 2024.
Explore 9EMC in 3D Show helices and sheets RCSB PDB PDBe
9EMC contains 126 α-helices and 126 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 15 | 1 | 1 |
| β-strand | 26 | 1 | 2 |
| α-helix | 31 | 1 | |
| β-strand | 32 | 1 | 2 |
| α-helix | 33 | 1 | |
| β-strand | 35-36 | 2 | 3 |
| β-strand | 39-40 | 2 | 3 |
| α-helix | 43-58 | 16 | |
| β-strand | 61 | 1 | 4 |
| β-strand | 65-69 | 5 | 5 |
| α-helix | 77-87 | 11 | |
| β-strand | 93-97 | 5 | 5 |
| α-helix | 98-101 | 4 | |
| α-helix | 108-118 | 11 | |
| β-strand | 120-124 | 5 | 6 |
| β-strand | 236-239 | 4 | 6 |
| α-helix | 240-246 | 7 | |
| α-helix | 273-288 | 16 | |
| β-strand | 292-296 | 5 | 6 |
| β-strand | 298-302 | 5 | 5 |
| α-helix | 304-306 | 3 | |
| β-strand | 308 | 1 | 7 |
| α-helix | 309-319 | 11 | |
| α-helix | 324-325 | 2 | |
| β-strand | 326-331 | 6 | 5 |
| β-strand | 336-337 | 2 | 8 |
| α-helix | 338 | 1 | |
| β-strand | 339 | 1 | 7 |
| β-strand | 345-346 | 2 | 8 |
| α-helix | 347-349 | 3 | |
| α-helix | 352-355 | 4 | |
| β-strand | 358-362 | 5 | 5 |
| α-helix | 364-367 | 4 | |
| α-helix | 368-381 | 14 | |
| β-strand | 386 | 1 | 9 |
| α-helix | 388-400 | 13 | |
| α-helix | 403-407 | 5 | |
| α-helix | 410-420 | 11 | |
| β-strand | 425 | 1 | 9 |
| α-helix | 427-436 | 10 | |
| β-strand | 438 | 1 | 10 |
| α-helix | 440-449 | 10 | |
| β-strand | 455 | 1 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 22 | 1 | 4 |
| β-strand | 33 | 1 | 12 |
| α-helix | 38 | 1 | |
| β-strand | 39 | 1 | 12 |
| α-helix | 40 | 1 | |
| β-strand | 42-43 | 2 | 13 |
| β-strand | 46-47 | 2 | 13 |
| α-helix | 50-65 | 16 | |
| β-strand | 68 | 1 | 14 |
| β-strand | 72-77 | 6 | 15 |
| α-helix | 83-94 | 12 | |
| β-strand | 100-104 | 5 | 15 |
| α-helix | 115-124 | 10 | |
| β-strand | 127-133 | 7 | 16 |
| β-strand | 238-243 | 6 | 16 |
| α-helix | 244-250 | 7 | |
| α-helix | 256-258 | 3 | |
| α-helix | 267-269 | 3 | |
| α-helix | 270-286 | 17 | |
| β-strand | 289-293 | 5 | 16 |
| β-strand | 295-299 | 5 | 15 |
| α-helix | 301-303 | 3 | |
| α-helix | 306-315 | 10 | |
| α-helix | 321-322 | 2 | |
| β-strand | 323-328 | 6 | 15 |
| β-strand | 330 | 1 | 17 |
| β-strand | 333-334 | 2 | 18 |
| β-strand | 341-342 | 2 | 18 |
| α-helix | 343-345 | 3 | |
| α-helix | 348-351 | 4 | |
| β-strand | 355-359 | 5 | 15 |
| α-helix | 360-362 | 3 | |
| α-helix | 364-377 | 14 | |
| β-strand | 382 | 1 | 19 |
| α-helix | 384-396 | 13 | |
| α-helix | 399-415 | 17 | |
| β-strand | 421 | 1 | 19 |
| α-helix | 423-432 | 10 | |
| β-strand | 434 | 1 | 5 |
| α-helix | 436-445 | 10 | |
| α-helix | 446-448 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RuvB-like 1 | A, B, C | protein | 459 | Homo sapiens | Q9Y265 (AlphaFold model) |
| RuvB-like 2 | D, E, F | protein | 481 | Homo sapiens | Q9Y230 (AlphaFold model) |
>9EMC_1 RuvB-like 1 (chains A, B, C) GSHMKIEEVKSTTKTQRIASHSHVKGLGLDESGLAKQAASGLVGQENAREACGVIVELIK SKKMAGRAVLLAGPPGTGKTALALAIAQELGSKVPFCPMVGSEVYSTEIKKTEVLMENFR RAIGLRIKETKEVYEGEVTELTPCETENPMGGYGKTISHVIIGLKTAKGTKQLKLDPSIF ESLQKERVEAGDVIYIEANSGAVKRQGRCDTYATEFDLEAEEYVPLPKGDVHKKKEIIQD VTLHDLDVANARPQGGQDILSMMGQLMKPKKTEITDKLRGEINKVVNKYIDQGIAELVPG VLFVDEVHMLDIECFTYLHRALESSIAPIVIFASNRGNCVIRGTEDITSPHGIPLDLLDR VMIIRTMLYTPQEMKQIIKIRAQTEGINISEEALNHLGEIGTKTTLRYSVQLLTPANLLA KINGKDSIEKEHVEEISELFYDAKSSAKILADQQDKYMK
>9EMC_2 RuvB-like 2 (chains D, E, F) MADLNWISAGHAIADVGTMATVTATTKVPEIRDVTRIERIGAHSHIRGLGLDDALEPRQA SQGMVGQLAARRAAGVVLEMIREGKIAGRAVLIAGQPGTGKTAIAMGMAQALGPDTPFTA IAGSEIFSLEMSKTEALTQAFRRSIGVRIKEETEIIEGEVVEIQIDRPATGTGSKVGKLT LKTTEMETIYDLGTKMIESLTKDKVQAGDVITIDKATGKISKLGRSFTRARDYDAMGSQT KFVQCPDGELQKRKEVVHTVSLHEIDVINSRTQGFLALFSGDTGEIKSEVREQINAKVAE WREEGKAEIIPGVLFIDEVHMLDIESFSFLNRALESDMAPVLIMATNRGITRIRGTSYQS PHGIPIDLLDRLLIVSTTPYSEKDTKQILRIRCEEEDVEMSEDAYTVLTRIGLETSLRYA IQLITAASLVCRKRKGTEVQVDDIKRVYSLFLDESRSTQYMKEYQDAFLFNELKGETMDT S
Mechanism of allosteric inhibition of RUVBL1-RUVBL2 by the small-molecule CB-6644. Garcia-Martin, C., Lopez-Perrote, A., Boskovic, J. et al. Cell Rep Phys Sci (2024). DOI 10.1016/j.xcrp.2024.101982
Other PDB entries of the same protein (UniProt Q9Y265 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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